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Database: UniProt
Entry: Q9TLR1_CYACA
LinkDB: Q9TLR1_CYACA
Original site: Q9TLR1_CYACA 
ID   Q9TLR1_CYACA            Unreviewed;        61 AA.
AC   Q9TLR1;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Photosystem II reaction center protein Z {ECO:0000256|ARBA:ARBA00021665, ECO:0000256|RuleBase:RU003472};
GN   Name=ycf9 {ECO:0000313|EMBL:AAF12886.1};
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AAF12886.1}.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771 {ECO:0000313|EMBL:AAF12886.1};
RN   [1] {ECO:0000313|EMBL:AAF12886.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RK1 {ECO:0000313|EMBL:AAF12886.1};
RA   Gloeckner G., Rosenthal A., Valentin K.;
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAF12886.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RK1 {ECO:0000313|EMBL:AAF12886.1};
RX   PubMed=11040290;
RA   Glockner G., Rosenthal A., Valentin K.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
CC   -!- FUNCTION: Controls the interaction of photosystem II (PSII) cores with
CC       the light-harvesting antenna, regulates electron flow through the 2
CC       photosystem reaction centers. PSII is a light-driven water
CC       plastoquinone oxidoreductase, using light energy to abstract electrons
CC       from H(2)O, generating a proton gradient subsequently used for ATP
CC       formation. {ECO:0000256|RuleBase:RU003472}.
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC       PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC       PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-
CC       evolving complex and a large number of cofactors. It forms dimeric
CC       complexes. {ECO:0000256|ARBA:ARBA00038734}.
CC   -!- SIMILARITY: Belongs to the PsbZ family. {ECO:0000256|ARBA:ARBA00008367,
CC       ECO:0000256|RuleBase:RU003472}.
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DR   EMBL; AF022186; AAF12886.1; -; Genomic_DNA.
DR   RefSeq; NP_045208.1; NC_001840.1.
DR   AlphaFoldDB; Q9TLR1; -.
DR   GeneID; 800123; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR   Gene3D; 1.10.287.740; Photosystem II PsbZ, reaction centre; 1.
DR   InterPro; IPR002644; PSII_PsbZ.
DR   InterPro; IPR036512; PSII_PsbZ_sf.
DR   Pfam; PF01737; Ycf9; 1.
DR   SUPFAM; SSF161055; PsbZ-like; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:AAF12886.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW   ECO:0000256|RuleBase:RU003472};
KW   Photosystem II {ECO:0000256|ARBA:ARBA00023276,
KW   ECO:0000256|RuleBase:RU003472}; Plastid {ECO:0000313|EMBL:AAF12886.1};
KW   Reaction center {ECO:0000256|ARBA:ARBA00022469,
KW   ECO:0000256|RuleBase:RU003472};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU003472};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003472};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   61 AA;  6911 MW;  C4C44154EEAFF83E CRC64;
     MSILLQFFII SIIFFSLILV ILVPSQLSLQ SGWQVSKSRF IALFTIWASM ILISGFISVF
     V
//
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